Hemoglobin & Oxygen Binding

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6 Terms

1
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Hemoglobin structure

  • 2 pairs of polypeptide chains

  • 4 heme groups

2
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Heme structure

  • 1 heme → 1 Oxygen

3
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Oxygen Curve

  • T = Tense

    • low affinity

  • R = relaxed

    • high affinity

4
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Bohr Effect

  • Increased CO2 + acidity → decreased affinity (right shift)

    • More oxygen released

  • Left shift = high affinity → Hb holds O2

  • Right Shift = low affinity → more O2 released

5
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<p>high pO2 </p>

high pO2

hemoglobin binds O2

6
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<p>low pO2 </p>

low pO2

hemoglobin releases O2